Xylanase and β-Xylosidase from Penicillium janczewskii: Production, Physico-chemical Properties, and Application of the Crude Extract to Pulp Biobleaching

Terrasan, César Rafael Fanchini; Temer, Beatriz; Sarto, Camila; Júnior, Francides G. Silva; Carmona, Eleonora Cano

doi:10.15376/biores.8.1.1292-1305

Cited by 24 publications

(17 citation statements)

References 28 publications

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“…The optimum temperature of the xylanase was similar to that observed for the free-enzyme, while for the α-L-arabinofuranosidase and β-xylosidase the optimum temperature was increased by 5 °C in relation to those previously observed for the free enzymes [28,29].…”

Section: Derivative Characterizationsupporting

confidence: 79%

“…Production of xylanase, β-xylosidase and α-L-arabinofuranosidase has been previously optimized [28,29] but other enzymes from the xylanolytic complex may also be produced by this fungal strain since SDS-PAGE revealed the presence of several extracellular proteins (Fig. 1) [28].…”

Section: Enzyme Immobilizationmentioning

confidence: 99%

“…1) [28]. Due to their potential application in many bioprocesses, several activation protocols, techniques and strategies were evaluated in order to optimize the concomitant immobilization of the crude extracellular xylanase, β-xylosidase and α-L-arabinofuranosidase on agarose-based supports, which have been widely used for immobilizing different enzymes [30].…”

Section: Enzyme Immobilizationmentioning

confidence: 99%

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Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis

Terrasan

Trobo-Maseda

Moreno-Pérez

et al. 2016

Process Biochemistry

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Differently activated agarose-based supports were evaluated for co-immobilization of a crude extract from Penicillium janczewskii containing xylanase, β-xylosidase and α-Larabinofuranosidase activities. Adequately selecting support and immobilization conditions (8 h, using agarose with 10% crosslinking) increased enzyme levels substantially, mainly in relation to the xylanase (2-fold). A coating with dextran aldehyde MW 6,000 Da, partially oxidized, covalently attached the enzymes to the support. Optimum activity was verified in the pH range 2-4, and at 50, 65 and 80 °C for the xylanase, α-L-arabinofuranosidase and β-xylosidase, 2 respectively. The xylanase was highly thermostable retaining more than 70% of activity even after 24 h incubation at 60 and 70 °C; and at 80 °C its half-life was 1.7 h. The half-lives of the β-xylosidase and α-L-arabinofuranosidase at 50 °C were 2.3 and 3.8 h, respectively. The coimmobilization of the enzymes on a single support give raise to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the α-Larabinofuranosidase presented high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles.

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Section: Derivative Characterizationsupporting

confidence: 79%

Section: Enzyme Immobilizationmentioning

confidence: 99%

Section: Enzyme Immobilizationmentioning

confidence: 99%

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Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis

Terrasan

Trobo-Maseda

Moreno-Pérez

et al. 2016

Process Biochemistry

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“…Enzyme immobilization P. janczewskii was isolated from soil of the Brazilian Rainforest [27] and characterized as an excellent producer of xylanolytic enzymes in the absence of cellulases [13]. Production of xylanase, ␤-xylosidase and ␣-l-arabinofuranosidase has been previously optimized [28,29] but other enzymes from the xylanolytic complex may also be produced by this fungal strain since SDS-PAGE revealed the presence of several extracellular proteins ( Fig. 1) [28].…”

Section: Methodsmentioning

confidence: 99%

“…Production of xylanase, ␤-xylosidase and ␣-l-arabinofuranosidase has been previously optimized [28,29] but other enzymes from the xylanolytic complex may also be produced by this fungal strain since SDS-PAGE revealed the presence of several extracellular proteins ( Fig. 1) [28]. Due to their potential application in many bioprocesses, several activation protocols, techniques and strategies were evaluated in order to optimize the concomitant immobilization of the crude extracellular xylanase, ␤-xylosidase and ␣-l-arabinofuranosidase on agarosebased supports, which have been widely used for immobilizing different enzymes [30].…”

Section: Methodsmentioning

confidence: 99%

Sodium hydrosulfide prevents hypertension and increases in vascular endothelial growth factor and soluble fms-like tyrosine kinase-1 in hypertensive pregnant rats

Possomato-Vieira

Gonçalves-Rizzi

Graça

et al. 2016

Naunyn-Schmiedeberg's Arch Pharmacol

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Sodium hydrosulfide (NaHS) has presented antihypertensive and antioxidant effects and may reduce circulating soluble fms-like tyrosine kinase-1 (sFlt-1). We examined whether NaHS prevents maternal and fetal detrimental changes in a model of hypertension in pregnancy induced by N(G)-nitro-L-arginine methyl ester (L-NAME). Forty pregnant rats were divided into four groups (n = 10 per group): Norm-Preg, Preg + NaHS, HTN-Preg, or HTN-Preg + NaHS. Systolic blood pressure (SBP), number of viable fetuses, litter size, pups, and placentae weights were recorded. Circulating plasma sFlt-1, vascular endothelial growth factor (VEGF), myeloperoxidase (MPO), trolox equivalent antioxidant capacity (TEAC) levels, and biochemical determinants of nitric oxide (NO) formation were assessed. SBP values were elevated in the HTN-Preg group on gestational days 16, 18, and 20. However, HTN-Preg + NaHS group presented lower SBP values on days 18 and 20. Lower number of viable fetuses and litter size were found only in HTN-Preg group compared to other. Reductions in placental weight were found in HTN-Preg and HTN-Preg + NaHS groups. Increases in fetal weight were found only in Preg + NaHS group. Increases in circulating sFlt-1 and VEGF levels were observed only in HTN-Preg group compared to other. Higher MPO and lower TEAC plasma levels were found in HTN-Preg + NaHS and HTN-Preg groups. NO was diminished in HTN-Preg animals, and NaHS treatment increased NO levels only in hypertensive pregnant animals. Treatment with NaHS prevents hypertension in pregnancy and concomitantly reduces circulating plasma sFlt-1 and VEGF levels; this correlates with improved litter size with more viable fetuses and increase in NO levels. However, these beneficial effects presented no relation with oxidative stress.

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Engineered GH11 xylanases from Orpinomyces sp. PC‐2 improve techno‐functional properties of bread dough

et al. 2018

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Xylanase and β-Xylosidase from Penicillium janczewskii: Production, Physico-chemical Properties, and Application of the Crude Extract to Pulp Biobleaching

Cited by 24 publications

References 28 publications

Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis

Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis

Sodium hydrosulfide prevents hypertension and increases in vascular endothelial growth factor and soluble fms-like tyrosine kinase-1 in hypertensive pregnant rats

Engineered GH11 xylanases from Orpinomyces sp. PC‐2 improve techno‐functional properties of bread dough

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